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Volumn 17, Issue 2, 2012, Pages 2015-2029

3D-QSAR studies of dihydropyrazole and dihydropyrrole derivatives as inhibitors of human mitotic kinesin Eg5 based on molecular docking

Author keywords

3D QSAR; Eg5 inhibitors; LigandFit docking

Indexed keywords

KIF11 PROTEIN, HUMAN; KINESIN; LIGAND; PYRROLE DERIVATIVE; PYRROLINE;

EID: 84863148303     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules17022015     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy, A.; Lane, H.A.; d'Herin, P.; Harper, M.; Kress, M.; Nigg, E.A. Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 1995, 83, 1159-1169.
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    D'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 2
    • 0347928860 scopus 로고    scopus 로고
    • Targeting the kinesin Eg5 to monitor siRNA transfection in mammalian cells
    • Weil, D.; Garcon, L.; Harper, M.; Dumenil, D.; Dautry, F.; Kress, M. Targeting the kinesin Eg5 to monitor siRNA transfection in mammalian cells. Biotechniques 2002, 33, 1244-1248. (Pubitemid 36008179)
    • (2002) BioTechniques , vol.33 , Issue.6 , pp. 1244-1248
    • Weil, D.1    Garcon, L.2    Harper, M.3    Dumenil, D.4    Dautry, F.5    Kress, M.6
  • 3
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T.U.; Kapoor, T.M.; Haggarty, S.J.; King, R.W.; Schreiber, S.L.; Mitchison, T.J. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 1999, 286, 971-974.
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 4
    • 0036752261 scopus 로고    scopus 로고
    • Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5
    • DOI 10.1016/S1074-5521(02)00212-0, PII S1074552102002120
    • Maliga, Z.; Kapoor, T.M.; Mitchison, T.J. Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5. Chem. Biol. 2002, 9, 989-996. (Pubitemid 35273719)
    • (2002) Chemistry and Biology , vol.9 , Issue.9 , pp. 989-996
    • Maliga, Z.1    Kapoor, T.M.2    Mitchison, T.J.3
  • 5
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • Turner, J.; Anderson, R.; Guo, J.; Beraud, C.; Fletterick, R.; Sakowicz, R. Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. J. Biol. Chem. 2001, 276, 25496-25502.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Guo, J.3    Beraud, C.4    Fletterick, R.5    Sakowicz, R.6
  • 7
    • 33745867225 scopus 로고    scopus 로고
    • S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression
    • DOI 10.1074/jbc.M511735200
    • Skoufias, D.A.; DeBonis, S.; Saoudi, Y.; Lebeau, L.; Crevel, I.; Cross, R.; Wade, R.H.; Hackney, D.; Kozielski, F. S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression. J. Biol. Chem. 2006, 281, 17559-17569. (Pubitemid 44035555)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17559-17569
    • Skoufias, D.A.1    DeBonis, S.2    Saoudi, Y.3    Lebeau, L.4    Crevel, I.5    Cross, R.6    Wade, R.H.7    Hackney, D.8    Kozielski, F.9
  • 8
    • 22144463476 scopus 로고    scopus 로고
    • Development and biological evaluation of potent and specific inhibitors of mitotic kinesin Eg5
    • DOI 10.1002/cbic.200500005
    • Gartner, M.; Sunder-Plassmann, N.; Seiler, J.; Utz, M.; Vernos, I.; Surrey, T.; Giannis, A. Development and biological evaluation of potent and specific inhibitors of mitotic Kinesin Eg5. ChemBioChem 2005, 6, 1173-1177. (Pubitemid 40978175)
    • (2005) ChemBioChem , vol.6 , Issue.7 , pp. 1173-1177
    • Gartner, M.1    Sunder-Plassmann, N.2    Seiler, J.3    Utz, M.4    Vernos, I.5    Surrey, T.6    Giannis, A.7
  • 9
    • 38449098965 scopus 로고    scopus 로고
    • Screening for inhibitors of microtubule-associated motor proteins
    • Kozielski, F.; DeBonis, S.; Skoufias, D.A. Screening for inhibitors of microtubule-associated motor proteins. Methods Mol. Med. 2007, 137, 189-207.
    • (2007) Methods Mol. Med. , vol.137 , pp. 189-207
    • Kozielski, F.1    Debonis, S.2    Skoufias, D.A.3
  • 10
    • 0345688612 scopus 로고    scopus 로고
    • Mechanisms of Taxol resistance related to microtubules
    • DOI 10.1038/sj.onc.1206934, Drug Resistance
    • Orr, G.A.; Verdier-Pinard, P.; McDaid, H.; Horwitz, S.B. Mechanisms of Taxol resistance related to microtubules. Oncogene 2003, 22, 7280-7295. (Pubitemid 37487160)
    • (2003) Oncogene , vol.22 , Issue.47 REV. ISS. 6 , pp. 7280-7295
    • Orr, G.A.1    Verdier-Pinard, P.2    McDaid, H.3    Horwitz, S.B.4
  • 11
    • 77649191871 scopus 로고    scopus 로고
    • Microtubules and resistance to tubulin-binding agents
    • Kavallaris, M. Microtubules and resistance to tubulin-binding agents. Nat. Rev. Cancer 2010, 10, 194-204.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 194-204
    • Kavallaris, M.1
  • 12
    • 79952778930 scopus 로고    scopus 로고
    • Structure-activity relationship and multidrug resistance study of new S-trityl-L-cysteine derivatives as inhibitors of Eg5
    • Kaan, H.Y.; Weiss, J.; Menger, D.; Ulaganathan, V.; Tkocz, K.; Laggner, C.; Popowycz, F.; Joseph, B.; Kozielski, F. Structure-activity relationship and multidrug resistance study of new S-trityl-L-cysteine derivatives as inhibitors of Eg5. J. Med. Chem. 2011, 54, 1576-1586.
    • (2011) J. Med. Chem. , vol.54 , pp. 1576-1586
    • Kaan, H.Y.1    Weiss, J.2    Menger, D.3    Ulaganathan, V.4    Tkocz, K.5    Laggner, C.6    Popowycz, F.7    Joseph, B.8    Kozielski, F.9
  • 14
    • 45649085011 scopus 로고    scopus 로고
    • Validating the mitotic kinesin Eg5 as a therapeutic target in pancreatic cancer cells and tumor xenografts using a specific inhibitor
    • Liu, M.; Yu, H.; Huo, L.; Liu, J.; Li, M.; Zhou, J. Validating the mitotic kinesin Eg5 as a therapeutic target in pancreatic cancer cells and tumor xenografts using a specific inhibitor. Biochem. Pharmacol. 2008, 76, 169-178.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 169-178
    • Liu, M.1    Yu, H.2    Huo, L.3    Liu, J.4    Li, M.5    Zhou, J.6
  • 15
    • 77949541280 scopus 로고    scopus 로고
    • The first highly stereoselective approach to the mitotic kinesin Eg5 inhibitor HR22C16 and its analogues
    • Xiao, S.; Shi, X.-X. The first highly stereoselective approach to the mitotic kinesin Eg5 inhibitor HR22C16 and its analogues. Tetrahedron: Asymmetry 2010, 21, 226-231.
    • (2010) Tetrahedron: Asymmetry , vol.21 , pp. 226-231
    • Xiao, S.1    Shi, X.-X.2
  • 16
    • 33646175956 scopus 로고    scopus 로고
    • Kinesin spindle protein (KSP) inhibitors. Part 4:1 Structure-based design of 5-alkylamino-3,5-diaryl-4,5-dihydropyrazoles as potent, water-soluble inhibitors of the mitotic kinesin KSP
    • Cox, C.D.; Torrent, M.; Breslin, M.J.; Mariano, B.J.; Whitman, D.B.; Coleman, P.J.; Buser, C.A.; Walsh, E.S.; Hamilton, K.; Schaber, M.D. Kinesin spindle protein (KSP) inhibitors. Part 4:1 Structure-based design of 5-alkylamino-3,5-diaryl-4,5-dihydropyrazoles as potent, water-soluble inhibitors of the mitotic kinesin KSP. Bioorg. Med. Chem. Lett. 2006, 16, 3175-3179.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 3175-3179
    • Cox, C.D.1    Torrent, M.2    Breslin, M.J.3    Mariano, B.J.4    Whitman, D.B.5    Coleman, P.J.6    Buser, C.A.7    Walsh, E.S.8    Hamilton, K.9    Schaber, M.D.10
  • 19
    • 5444274954 scopus 로고    scopus 로고
    • Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5
    • DOI 10.1021/bi049264e
    • Brier, S.; Lemaire, D.; Debonis, S.; Forest, E.; Kozielski, F. Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5. Biochemistry 2004, 43, 13072-13082. (Pubitemid 39362777)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13072-13082
    • Brier, S.1    Lemaire, D.2    DeBonis, S.3    Forest, E.4    Kozielski, F.5
  • 20
    • 72449183762 scopus 로고    scopus 로고
    • An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex
    • Yi Kristal Kaan, H.; Ulaganathan, V.; Hackney, D.D.; Kozielski, F. An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex. Biochem. J. 2010, 425, 55-60.
    • (2010) Biochem. J. , vol.425 , pp. 55-60
    • Yi Kristal Kaan, H.1    Ulaganathan, V.2    Hackney, D.D.3    Kozielski, F.4
  • 22
    • 38949179546 scopus 로고    scopus 로고
    • Proteome analysis of apoptosis signaling by S-trityl-L-cysteine, a potent reversible inhibitor of human mitotic kinesin Eg5
    • DOI 10.1002/pmic.200700534
    • Kozielski, F.; Skoufias, D.A.; Indorato, R.L.; Saoudi, Y.; Jungblut, P.R.; Hustoft, H.K.; Strozynski, M.; Thiede, B. Proteome analysis of apoptosis signaling by S-trityl-L-cysteine, a potent reversible inhibitor of human mitotic kinesin Eg5. Proteomics 2008, 8, 289-300. (Pubitemid 351212328)
    • (2008) Proteomics , vol.8 , Issue.2 , pp. 289-300
    • Kozielski, F.1    Skoufias, D.A.2    Indorato, R.-L.3    Saoudi, Y.4    Jungblut, P.R.5    Hustoff, H.K.6    Strozynski, M.7    Thiede, B.8
  • 24
    • 0030771347 scopus 로고    scopus 로고
    • QSAR and 3D QSAR in drug design. Part 1: Methodology
    • DOI 10.1016/S1359-6446(97)01079-9, PII S1359644697010799
    • Kubinyi, H. QSAR and 3D QSAR in drug design Part 1: Methodology. Drug Discov. Today 1997, 2, 457-467. (Pubitemid 27450428)
    • (1997) Drug Discovery Today , vol.2 , Issue.11 , pp. 457-467
    • Kubinyi, H.1
  • 25
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins
    • Cramer, R.D.; Patterson, D.E.; Bunce, J.D. Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins. J. Am. Chem. Soc. 1988, 110, 5959-5967.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5959-5967
    • Cramer, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 26
    • 0027944195 scopus 로고
    • Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity
    • DOI 10.1021/jm00050a010
    • Klebe, G.; Abraham, U.; Mietzner, T. Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity. J. Med. Chem. 1994, 37, 4130-4146. (Pubitemid 24379702)
    • (1994) Journal of Medicinal Chemistry , vol.37 , Issue.24 , pp. 4130-4146
    • Klebe, G.1    Abraham, U.2    Mietzner, T.3
  • 27
    • 33144490688 scopus 로고    scopus 로고
    • 3D-QSAR studies of farnesyltransferase inhibitors: A comparative molecular field analysis approach
    • DOI 10.1016/j.bmcl.2006.01.019, PII S0960894X06000084
    • Puntambekar, D.; Giridhar, R.; Yadav, M.R. 3D-QSAR studies of farnesyltransferase inhibitors: A comparative molecular field analysis approach. Bioorg. Med. Chem. Lett. 2006, 16, 1821-1827. (Pubitemid 43267358)
    • (2006) Bioorganic and Medicinal Chemistry Letters , vol.16 , Issue.7 , pp. 1821-1827
    • Puntambekar, D.1    Giridhar, R.2    Yadav, M.R.3
  • 28
    • 8444236789 scopus 로고    scopus 로고
    • CoMFA and CoMSIA studies of nAChRs ligands: Epibatidine analogues
    • DOI 10.1002/qsar.200330851
    • Zhang, H.; Liu, C.; Li, H. CoMFA and CoMSIA Studies of nAChRs Ligands: Epibatidine Analogues. QSAR Comb. Sci. 2004, 23, 80-88. (Pubitemid 39486051)
    • (2004) QSAR and Combinatorial Science , vol.23 , Issue.2-3 , pp. 80-88
    • Zhang, H.1    Liu, C.2    Li, H.3
  • 29
    • 79958146739 scopus 로고    scopus 로고
    • Rational questing for potential novel inhibitors of FabK from Streptococcus pneumoniae by combining FMO calculation, CoMFA 3D-QSAR modeling and virtual screening
    • Zhang, Q.; Yu, C.; Min, J.; Wang, Y.; He, J.; Yu, Z. Rational questing for potential novel inhibitors of FabK from Streptococcus pneumoniae by combining FMO calculation, CoMFA 3D-QSAR modeling and virtual screening. J. Mol. Model. 2010, 17, 1483-1492.
    • (2010) J. Mol. Model. , vol.17 , pp. 1483-1492
    • Zhang, Q.1    Yu, C.2    Min, J.3    Wang, Y.4    He, J.5    Yu, Z.6
  • 30
    • 39449137882 scopus 로고    scopus 로고
    • Human microsomal prostaglandin e synthase-1 (mPGES-1) binding with inhibitors and the quantitative structure-activity correlation
    • DOI 10.1021/ci700315c
    • AbdulHameed, M.D.; Hamza, A.; Liu, J.; Huang, X.; Zhan, C.G. Human microsomal prostaglandin E synthase-1 (mPGES-1) binding with inhibitors and the quantitative structure-activity correlation. J. Chem. Inf. Model. 2008, 48, 179-185. (Pubitemid 351271063)
    • (2008) Journal of Chemical Information and Modeling , vol.48 , Issue.1 , pp. 179-185
    • Abdul Hameed, M.D.M.1    Hamza, A.2    Liu, J.3    Huang, X.4    Zhan, C.-G.5
  • 31
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites
    • DOI 10.1016/S1093-3263(02)00164-X, PII S109332630200164X
    • Venkatachalam, C.M.; Jiang, X.; Oldfield, T.; Waldman, M. LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites. J. Mol. Graph. Model. 2003, 21, 289-307. (Pubitemid 35441326)
    • (2003) Journal of Molecular Graphics and Modelling , vol.21 , Issue.4 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 32
    • 84863163370 scopus 로고    scopus 로고
    • Application of structure-based alignment methods for 3D QSAR analyses
    • Wiley-VCH Verlag GmbH & Co. KGaA: Weinheim, Germany
    • Sippl, W. Application of Structure-Based Alignment Methods for 3D QSAR Analyses. In Pharmacophores and Pharmacophore Searches; Wiley-VCH Verlag GmbH & Co. KGaA: Weinheim, Germany, 2006; pp. 223-249.
    • (2006) Pharmacophores and Pharmacophore Searches , pp. 223-249
    • Sippl, W.1
  • 33
    • 33846108633 scopus 로고    scopus 로고
    • BindingDB: A web-accessible database of experimentally determined protein-ligand binding affinities
    • DOI 10.1093/nar/gkl999
    • Liu, T.; Lin, Y.; Wen, X.; Jorissen, R.N.; Gilson, M.K. BindingDB: A web-accessible database of experimentally determined protein-ligand binding affinities. Nucleic Acids Res. 2007, 35, D198-D201. (Pubitemid 46056198)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL. 1
    • Liu, T.1    Lin, Y.2    Wen, X.3    Jorissen, R.N.4    Gilson, M.K.5


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